Search results for " Glycoproteins"

showing 10 items of 329 documents

Combining two mutations of human interleukin-6 that affect gp130 activation results in a potent interleukin-6 receptor antagonist on human myeloma ce…

1995

The pleiotropic cytokine interleukin-6 (IL-6) interacts with the specific ligand binding subunit (IL-6R alpha) of the IL-6 receptor, and this complex associates with the signal-transducing subunit gp130 (IL-6R beta). Human IL-6 acts on human and murine cells, whereas murine IL-6 is only active on murine cells. The construction of a set of chimeric human/murine IL-6 proteins has recently allowed us to define a region (residues 43-55) within the human IL-6 protein, which is important for the interaction with gp130. Subdividing this region shows that mainly residues 50-55 of the human IL-6 are necessary for this interaction. Recently, another human IL-6 double mutant (Q159E and T162P) showed r…

Protein ConformationProtein subunitmedicine.medical_treatmentMutantMolecular Sequence DataBiologyBiochemistryMiceAntigenAntigens CDmedicineCytokine Receptor gp130Tumor Cells CulturedAnimalsHumansPoint MutationInterleukin 6ReceptorMolecular BiologyMembrane GlycoproteinsBase SequenceInterleukin-6Wild typeCell BiologyReceptors InterleukinGlycoprotein 130Molecular biologyReceptors Interleukin-6CytokineOligodeoxyribonucleotidesbiology.proteinMultiple MyelomaThe Journal of biological chemistry
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Identification of Single Amino Acid Residues of Human IL-6 Involved in Receptor Binding and Signal Initiation

1996

The pleiotropic cytokine interleukin-6 (IL-6) has been predicted to be a protein with four antiparallel alpha-helices. On target cells, IL-6 interacts with a specific ligand binding receptor subunit (IL-6R), and this complex associates with the signal-transducing subunit gp130. Human IL-6 acts on human and murine cells, whereas murine IL-6 is only active on murine cells. The construction of chimeric human/murine IL-6 proteins has allowed us to define a region (residues 77-95, region 2c) within the human IL-6 protein that is important for IL-6R binding and a region (residues 50-55, region 2a2) that is important for IL-6R dependent gp130 interaction. Guided by sequence alignment and molecular…

Protein ConformationRecombinant Fusion ProteinsProtein subunitMolecular Sequence DataImmunologySequence alignmentPlasma protein bindingBiologyLigandsMiceStructure-Activity RelationshipProtein structureAntigens CDVirologyCytokine Receptor gp130AnimalsHumansPoint MutationAmino Acid SequenceAmino AcidsReceptorPeptide sequenceMembrane GlycoproteinsInterleukin-6Receptors InterleukinCell BiologyGlycoprotein 130Receptors Interleukin-6BiochemistryMutagenesis Site-DirectedSignal transductionSequence AlignmentProtein BindingSignal TransductionJournal of Interferon & Cytokine Research
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The Recent Crystal Structure of Human Tyrosinase Related Protein 1 (HsTYRP1) Solves an Old Problem and Poses a New One

2017

Show your metal: l-Tyrosine is converted into the protective antioxidative polymer melanin in a sequence of reactions. In humans, the catalytic pathway starts with the tyrosinase HsTYR and two tyrosinase-related proteins HsTYRP1 and HsTYRP2. All three enzymes have the same active site but the latter two contain two zinc ions instead of copper ions.

Protein ConformationTyrosinasechemistry.chemical_elementNanotechnologyZincCrystallography X-Ray010402 general chemistry01 natural sciencesAntioxidantsCatalysisMelaninProtein structureCatalytic DomainHumansTYRP1MelanosomeMelaninschemistry.chemical_classificationMembrane Glycoproteinsbiology010405 organic chemistryActive siteGeneral ChemistryCombinatorial chemistry0104 chemical sciencesZincEnzymechemistrybiology.proteinTyrosineOxidoreductasesCopperAngewandte Chemie International Edition
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The membrane proximal cytokine receptor domain of the human interleukin-6 receptor is sufficient for ligand binding but not for gp130 association.

1998

Interleukin-6 (IL-6) belongs to the family of the "four-helix bundle" cytokines. The extracellular parts of their receptors consist of several Ig- and fibronectin type III-like domains. Characteristic of these receptors is a cytokine-binding module consisting of two such fibronectin domains defined by a set of four conserved cysteines and a tryptophan-serine-X-tryptophan-serine (WSXWS) sequence motif. On target cells, IL-6 binds to a specific IL-6 receptor (IL-6R), and the complex of IL-6.IL-6R associates with the signal transducing protein gp130. The IL-6R consists of three extracellular domains. The NH2-terminal Ig-like domain is not needed for ligand binding and signal initiation. Here w…

Protein FoldingProtein ConformationEnzyme-Linked Immunosorbent AssayPlasma protein bindingImmunoglobulin domainBiologyLigandsBiochemistryHAMP domainAntigens CDCytokine Receptor gp130HumansMolecular BiologyDNA PrimersMembrane GlycoproteinsBase SequenceInterleukin-6Cell BiologyHydrogen-Ion ConcentrationGlycoprotein 130Precipitin TestsReceptors Interleukin-6Recombinant ProteinsCell biologyKineticsBiochemistryMATH domainSignal transductionCytokine receptorBinding domainProtein BindingSignal TransductionThe Journal of biological chemistry
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Different protein turnover of interleukin-6-type cytokine signalling components.

1999

Interleukin (IL)-6 and IL-6-type cytokines signal through the gp130/Jak/STAT signal transduction pathway. The key components involved are the signal transducing receptor subunit gp130, the Janus kinases Jak1, Jak2 and Tyk2, STAT1 and STAT3 of the family of signal transducers and activators of transcription, the protein tyrosine phosphatase SHP2 and the suppressors of cytokine signalling SOCS1, SOCS2 and SOCS3. Whereas considerable information has been accumulated concerning the time-course of activation for the individual signalling molecules, data on the availability of the proteins involved in IL-6-type cytokine signal transduction are scarce. Nevertheless, availability of these molecules…

Protein Tyrosine Phosphatase Non-Receptor Type 11Protein tyrosine phosphataseBiologyBiochemistrySuppressor of cytokine signallingAntigens CDCytokine Receptor gp130Membrane GlycoproteinsSuppressor of cytokine signaling 1Interleukin-6Protein Tyrosine Phosphatase Non-Receptor Type 6Intracellular Signaling Peptides and ProteinsJAK-STAT signaling pathwaySignal transducing adaptor proteinSTAT2 Transcription FactorProtein-Tyrosine KinasesGlycoprotein 130Recombinant ProteinsCell biologyDNA-Binding ProteinsSTAT1 Transcription FactorBiochemistryTrans-ActivatorsCytokinesSignal transductionProtein Tyrosine PhosphatasesJanus kinaseHalf-LifeSignal TransductionEuropean journal of biochemistry
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EBV-Induced Gene 3 Transcription Is Induced by TLR Signaling in Primary Dendritic Cells via NF-κB Activation

2005

Abstract The EBV-induced gene 3 (EBI3) is expressed in dendritic cells (DCs) and part of the cytokine IL-27 that controls Th cell development. However, its regulated expression in DCs is poorly understood. In the present study we demonstrate that EBI3 is expressed in splenic CD8−, CD8+, and plasmacytoid DC subsets and is induced upon TLR signaling. Cloning and functional analysis of the EBI3 promoter using in vivo footprinting and mutagenesis showed that stimulation via TLR2, TLR4, and TLR9 transactivated the promoter in primary DCs via NF-κB and Ets binding sites at −90 and −73 bp upstream of the transcriptional start site, respectively. Furthermore, we observed that NF-κB p50/p65 and PU.1…

RNA Capsmedicine.medical_treatmentDNA Mutational AnalysisMolecular Sequence DataImmunologyAntigen-Presenting CellsReceptors Cell SurfaceBiologyCell LineMinor Histocompatibility AntigensJurkat CellsMiceCell Line TumorGene expressionmedicineAnimalsHumansImmunology and AllergyReceptors CytokinePromoter Regions GeneticGlycoproteinsMice KnockoutMembrane GlycoproteinsInnate immune systemBase SequenceToll-Like ReceptorsHEK 293 cellsNF-kappa BTLR9hemic and immune systemsEBI3Dendritic CellsMolecular biologyToll-Like Receptor 2Up-RegulationMice Inbred C57BLToll-Like Receptor 4Protein SubunitsTLR2CytokineGene Expression RegulationToll-Like Receptor 9NIH 3T3 CellsTLR4Protein BindingSignal TransductionThe Journal of Immunology
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Expression of the fibrinogen binding mannoprotein and the laminin receptor of Candida albicans in vitro and in infected tissues.

1996

We have previously reported a 37 kDa laminin-binding protein (p37) and a 58 kDa fibrinogen-binding mannoprotein (mp58) on the surface of Candida albicans. A few yeast cells expressed both functional receptors at the surface while germ tubes expressed a functional mp58 fibrinogen but not a functional p37 laminin receptor. These receptors were heterogeneously dispersed at the surface as shown by binding of rabbit antiserum to mp58 (PAb anti-mp58) and antiserum to the human high affinity laminin receptor. In this report we have used a dual fluorescence technique to determine if the two receptors colocalize, perhaps as part of a receptor complex. Fibrinogen was used as a probe for mp58 and poly…

Receptor complexBiologyImmunofluorescenceMicrobiologyReceptors LamininBacterial ProteinsLamininCandida albicansGeneticsmedicineAnimalsHumansReceptorCandida albicansFluorescent Antibody Technique IndirectMolecular BiologyAntibodies FungalAntiserumMembrane Glycoproteinsmedicine.diagnostic_testBinding proteinCandidiasisFibrinogen bindingFibrinogenbiology.organism_classificationMolecular biologyImmunohistochemistryBiochemistrybiology.proteinRabbitsCarrier ProteinsFEMS microbiology letters
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A New Type of Cytokine Receptor Antagonist Directly Targeting gp130

1998

The interleukin-6-type family of cytokines bind to receptor complexes that share gp130 as a common signal-transducing subunit. So far, receptor antagonists for interleukin-6-type cytokines have been constructed that still bind to the specific ligand binding subunit of the receptor complex, but have lost the ability to stimulate gp130. Such receptor antagonists compete for a specific receptor of a member of the cytokine family. Interleukin-6 only binds to gp130 when complexed with the interleukin-6 receptor that exists as a membrane bound and soluble molecule. Here we have constructed fusion proteins that consist of the soluble form of the human interleukin-6 receptor covalently linked to in…

Receptor complexRecombinant Fusion ProteinsNerve Tissue ProteinsOncostatin MBiologyLeukemia Inhibitory FactorBiochemistryAntigens CDCytokine Receptor gp130Enzyme-linked receptorHumansPoint Mutation5-HT5A receptorCiliary Neurotrophic FactorMolecular BiologyProtease-activated receptor 2Common gamma chainLymphokinesMembrane GlycoproteinsDose-Response Relationship DrugJanus kinase 1Interleukin-6digestive oral and skin physiologyCell BiologyReceptors Interleukin-6Growth Inhibitorsbiological factorsBiochemistryInterleukin-21 receptorCytokinesPeptidesCytokine receptorProtein BindingJournal of Biological Chemistry
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Soluble interleukin-6 receptor (sIL-6R) makes IL-6R negative T cell line respond to IL-6: it inhibits TNF production

2000

The receptor for interleukin-6 (IL-6) consists of two subunits: a ligand specific IL-6Ralpha and gp130 that is responsible for signal-transduction. A soluble form of the ligand specific chain was described that when complexed to IL-6 is capable of binding to the membrane-bound gp130 subunit and thus can elicit signal-transduction. This soluble receptor can act on cells that express only the gp130 but not the ligand-specific subunit of the IL-6R. This phenomenon, called trans-signaling, introduced a novel aspect of cytokine action. In this study we examined the response of Jurkat cells, that are known not to express IL-6Ralpha, to IL-6, the soluble IL-6 receptor (sIL-6R) and a covalent compl…

Recombinant Fusion ProteinsT-Lymphocytesmedicine.medical_treatmentT cellImmunologyBiologyJurkat cellsCell LineInterferon-gammaJurkat CellsAntigens CDCytokine Receptor gp130medicineHumansImmunology and AllergyInterferon gammaElméleti orvostudományokReceptorLymphotoxin-alphaMembrane GlycoproteinsInterleukin-6Tumor Necrosis Factor-alphaReceptors InterleukinOrvostudományokLigand (biochemistry)Glycoprotein 130Receptors Interleukin-6Molecular biologyCytokinemedicine.anatomical_structureSolubilityTumor necrosis factor alphamedicine.drug
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Mast cells counteract regulatory T-cell suppression through interleukin-6 and OX40/OX40L axis toward Th17-cell differentiation

2009

Abstract The development of inflammatory diseases implies inactivation of regulatory T (Treg) cells through mechanisms that still are largely unknown. Here we showed that mast cells (MCs), an early source of inflammatory mediators, are able to counteract Treg inhibition over effector T cells. To gain insight into the molecules involved in their interplay, we set up an in vitro system in which all 3 cellular components were put in contact. Reversal of Treg suppression required T cell–derived interleukin-6 (IL-6) and the OX40/OX40L axis. In the presence of activated MCs, concomitant abundance of IL-6 and paucity of Th1/Th2 cytokines skewed Tregs and effector T cells into IL-17–producing T cel…

Regulatory T cellmedicine.medical_treatmentCellular differentiationImmunologyPriming (immunology)chemical and pharmacologic phenomenaMice TransgenicMast cell; T regulatory cell; Immune responseBiologyLymphocyte ActivationT-Lymphocytes RegulatoryBiochemistryImmune toleranceMiceMice CongenicmedicineImmune ToleranceMast CellT regulatory cellImmune responseCells CulturedCell ProliferationAnimalInterleukin-6Experimental autoimmune encephalomyelitisInterleukin-17hemic and immune systemsCell DifferentiationT lymphocyteT-Lymphocytes Helper-InducerHematologyCell BiologyReceptors OX40medicine.diseaseCell biologyMice Inbred C57BLmedicine.anatomical_structureCytokineImmunologyAnimals; Cell Differentiation; Cell Proliferation; Cells Cultured; Immune Tolerance; Interleukin-17; Interleukin-6; Lymphocyte Activation; Mast Cells; Membrane Glycoproteins; Mice; Mice Congenic; Mice Inbred C57BL; Mice Transgenic; Receptors OX40; Signal Transduction; T-Lymphocytes Helper-Inducer; T-Lymphocytes Regulatory; Tumor Necrosis Factors; Hematology; Biochemistry; Cell Biology; ImmunologyInterleukin 17Membrane GlycoproteinTumor Necrosis FactorSignal Transduction
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